{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/25606"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/25606","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Pressure and temperature dependence of myoglobin kinetics","abstract":"Recombination kinetics of carbon monoxide to myoglobin and protoheme are measured from 0.1 MPa to 190 MPa (1 bar to 1.9 kbar) at temperatures from 290K to 60K using flash photolysis. The role of the protein structure is elucidated by comparison of myoglobin kinetics with those of protoheme whose active center is similar to myoglobin's but is not enclosed within a globular protein structure. The results are interpreted in terms of sequential Gibbs energy barriers along the ligand's reaction coordinate between the solvent and the binding site. Entropies and enthalpies of activation for each reaction step are extracted using this model. A nonrelaxed distribution of conformational states is used to explain the process below 200K. Tne distribution of activation enthalpies is derived from the data at high and low pressures. We determine that the influence of pressure on reaction kinetics below 200K is due to structural changes of the protein. The kinetics at higher temperatures indicate that the barriers to recombination caused by the protein structure are lessened at high pressure whereas the barrier at the solvent-protein boundary is increased by pressure.","abstract_html":"Recombination kinetics of carbon monoxide to myoglobin and protoheme are measured from 0.1 MPa to 190 MPa (1 bar to 1.9 kbar) at temperatures from 290K to 60K using flash photolysis. The role of the protein structure is elucidated by comparison of myoglobin kinetics with those of protoheme whose active center is similar to myoglobin's but is not enclosed within a globular protein structure. The results are interpreted in terms of sequential Gibbs energy barriers along the ligand's reaction coordinate between the solvent and the binding site. Entropies and enthalpies of activation for each reaction step are extracted using this model. A nonrelaxed distribution of conformational states is used to explain the process below 200K. Tne distribution of activation enthalpies is derived from the data at high and low pressures. We determine that the influence of pressure on reaction kinetics below 200K is due to structural changes of the protein. The kinetics at higher temperatures indicate that the barriers to recombination caused by the protein structure are lessened at high pressure whereas the barrier at the solvent-protein boundary is increased by pressure.","abstract_has_math":false,"creators":["Alberding, Neil Arnold"],"institution":null,"degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Physics","degree_department":null,"school":null,"contributors":["Frauenfelder, Hans"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-06-30T17:15:23Z","date_published":"2011-06-30T17:15:23Z","updated_at":"2026-07-22T22:25:24Z","subjects":["myoglobin kinetics","protein kinetics","recombination kinetics","carbon monoxide","protoheme"],"languages":["en"],"rights":["1978 Neil Arnold Alberding"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["311920"],"render_values":[{"text":"311920","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/25606","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Frauenfelder, Hans"]},{"key":"dc:creator","label":"Author","values":["Alberding, Neil Arnold"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-06-30T17:15:23Z","10000-01-01","1978"]},{"key":"dc:type","label":"Dc Type","values":["Dissertation / Thesis","text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Physics"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["myoglobin kinetics","protein kinetics","recombination kinetics","carbon monoxide","protoheme"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["1978 Neil Arnold Alberding"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["311920","http://hdl.handle.net/2142/25606"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Recombination kinetics of carbon monoxide to myoglobin and protoheme are measured from 0.1 MPa to 190 MPa (1 bar to 1.9 kbar) at temperatures from 290K to 60K using flash photolysis. The role of the protein structure is elucidated by comparison of myoglobin kinetics with those of protoheme whose active center is similar to myoglobin's but is not enclosed within a globular protein structure. The results are interpreted in terms of sequential Gibbs energy barriers along the ligand's reaction coordinate between the solvent and the binding site. Entropies and enthalpies of activation for each reaction step are extracted using this model. A nonrelaxed distribution of conformational states is used to explain the process below 200K. Tne distribution of activation enthalpies is derived from the data at high and low pressures. We determine that the influence of pressure on reaction kinetics below 200K is due to structural changes of the protein. The kinetics at higher temperatures indicate that the barriers to recombination caused by the protein structure are lessened at high pressure whereas the barrier at the solvent-protein boundary is increased by pressure.","Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-30T17:15:23Z No. of bitstreams: 1 1978_alberding.pdf: 2207022 bytes, checksum: c1f93b4d7ea383dbf5b15ceb93523f9a (MD5)","Made available in DSpace on 2011-06-30T17:15:23Z (GMT). No. of bitstreams: 1 1978_alberding.pdf: 2207022 bytes, checksum: c1f93b4d7ea383dbf5b15ceb93523f9a (MD5) Previous issue date: 1978","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-06-30T17:15:23Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:32:31-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis","Thesis","U of I Only"]},{"key":"dc:title","label":"Title","values":["Pressure and temperature dependence of myoglobin kinetics"]}]}],"canonical_facts":{"dc:contributor":["Frauenfelder, Hans"],"dc:creator":["Alberding, Neil Arnold"],"dc:date":["2011-06-30T17:15:23Z","10000-01-01","1978"],"dc:description":["Recombination kinetics of carbon monoxide to myoglobin and protoheme are measured from 0.1 MPa to 190 MPa (1 bar to 1.9 kbar) at temperatures from 290K to 60K using flash photolysis. The role of the protein structure is elucidated by comparison of myoglobin kinetics with those of protoheme whose active center is similar to myoglobin's but is not enclosed within a globular protein structure. The results are interpreted in terms of sequential Gibbs energy barriers along the ligand's reaction coordinate between the solvent and the binding site. Entropies and enthalpies of activation for each reaction step are extracted using this model. A nonrelaxed distribution of conformational states is used to explain the process below 200K. Tne distribution of activation enthalpies is derived from the data at high and low pressures. We determine that the influence of pressure on reaction kinetics below 200K is due to structural changes of the protein. The kinetics at higher temperatures indicate that the barriers to recombination caused by the protein structure are lessened at high pressure whereas the barrier at the solvent-protein boundary is increased by pressure.","Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-30T17:15:23Z No. of bitstreams: 1 1978_alberding.pdf: 2207022 bytes, checksum: c1f93b4d7ea383dbf5b15ceb93523f9a (MD5)","Made available in DSpace on 2011-06-30T17:15:23Z (GMT). No. of bitstreams: 1 1978_alberding.pdf: 2207022 bytes, checksum: c1f93b4d7ea383dbf5b15ceb93523f9a (MD5) Previous issue date: 1978","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-06-30T17:15:23Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:32:31-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis","Thesis","U of I Only"],"dc:identifier":["311920","http://hdl.handle.net/2142/25606"],"dc:language":["en"],"dc:rights":["1978 Neil Arnold Alberding"],"dc:subject":["myoglobin kinetics","protein kinetics","recombination kinetics","carbon monoxide","protoheme"],"dc:title":["Pressure and temperature dependence of myoglobin kinetics"],"dc:type":["Dissertation / Thesis","text"],"thesis:degree_discipline":["Physics"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."]},"updated_at":"2026-07-22T22:25:24Z"}